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Biomedical subjects

M Leppilampi

Publications and source records attributed to M Leppilampi.

4 recordsLinked to original sources

Carbonic anhydrase isoenzymes in isolated rat peripheral monocytes, tissue macrophages, and osteoclasts.

The presence of carbonic anhydrase isoenzymes I and II in rat monocytes and macrophagelike cells was studied using monospecific antisera against rat carbonic anhydrase I and II purified from red blood cells. CA II was strongly stained immunohistochemically in osteoclasts and macrophagelike cells in the umbilical cord. Foreign body giant cells, peritoneal macrophages, lung macrophages, and cultured peripheral monocytes, the presumed progenitor cells for osteoclasts, were negative with both antisera. Radioimmunoassay and immunoblotting similarly failed to demonstrate CA II in peripheral monocytes. The lack of CA in monocytes adds a new aspect to the discussion concerning the origin of osteoclasts and monocyte-mediated bone resorption.

Animals

Liberation of muscle carbonic anhydrase into serum during extensive exercise.

A sensitive radioimmunoassay method for measurement of human carbonic anhydrase III (CA III), a specific enzyme of skeletal muscle, was established. The effect of 24-h competitive running on serum CA III (S-CA III) was studied in healthy male long-distance runners. S-CA III increased gradually during the first 18 h 410-fold above the initial values. No further increase was observed during the last 6 h. On a day after the termination of the race S-CA III was not statistically different from the initial value. The activity of serum creatine kinase (S-CK) and lactate dehydrogenase (S-LDH) increased gradually through the run being elevated also 1 or 2 days afterward. The lack of increase in S-CA III during the last hours of exercise, and more rapid decrease afterward than in S-CK or S-LDH, may reflect differences in the rates of penetration through the sarcolemma and different degrees of injury in different fiber types or in the half-lives of these enzymes in serum.

Adult

Tumor-associated antigen Ca 125 before and during the treatment of ovarian carcinoma.

Serum concentrations of Ca 125, a tumor-associated antigen of epithelial ovarian cancer, were measured in 29 ovarian cancer patients before cytoreductive surgery and in 112 patients during and after treatment. Ca 125 levels were increased (greater than 30 IU/mL) in 89.8% of patients with clinically demonstrable ovarian tumors and were negative in 92.1% of clinically disease-free patients. Low levels of Ca 125 were associated with early clinical stages or a minimal tumor burden, and predicted a successful response to treatment and a low recurrence rate. High values indicated advanced disease and a poor response to cytotoxic chemotherapy. In 77% of patients the operation was explorative, with a preoperative Ca 125 level higher than 1000 IU/mL, whereas all the patients with values less than 100 IU/mL could be operated radically. Serum levels of Ca 125 were increased in similar frequency in epithelial, sex cord, and germ cell ovarian malignancies. The assay of Ca 125 seems to be a reliable noninvasive method for monitoring the presence and clinical behavior of ovarian cancer. Preoperative values have prognostic significance in predicting operability and response to chemotherapy.

Adenocarcinoma

Extramitochondrial protein synthesis in calf brain synaptosomes.

Isolated synaptosomes of calf brain cortex incorporated labelled amino acids into their mitochondrial, membranous and soluble proteins in an approximate ratio of 1:1:0.5 Synaptosomal protein synthesis was sensitive to ATP, noradrenaline, cycloheximide and puromycin, and together with mitochondrial protein synthesis, also to chloramphenicol, 2.4-dinitrophenol, KCN and hyperosmotic conditions. The absence of Na+ and K+ ions slightly inhibited both synaptosomal and mitochondrial protein synthesis. Using incorporated radioactivity as an indicator of synthesized proteins, the synaptosomal soluble proteins could be obtained in one large peak in gel and indicator of synthesized protein, the synaptosomal soluble proteins could be obtained in one large peak in gel filtration on Sephadex G-100 and G-25, and in two components in disc electrophoresis on a 7% polyacrylamide gel. An approximate molecular weight was calculated for the synthesized proteins using known proteins as standards, giving 15000-35000 in the gel filtration eluant, and 27000 and 36000 in the disc electrophoresis bands.

Adenosine Triphosphate